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Protein

Beta-1,3-N-acetylglucosaminyltransferase radical fringe

Gene

Rfng

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules. Modulates NOTCH1 activity by modifying O-fucose residues at specific EGF-like domains resulting in enhancement of NOTCH1 activation by DLL1 and JAG1 (By similarity). Inhibits Notch signaling in postmitotic neurons of the brain. It may play a role in adult brain and in neurogenesis (PubMed:11165380). It may play a role in limb development (By similarity).By similarity1 Publication

Catalytic activityi

Transfers a beta-D-GlcNAc residue from UDP-D-GlcNAc to the fucose residue of a fucosylated protein acceptor.

Cofactori

Mn2+By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei77SubstrateBy similarity1
Binding sitei150SubstrateBy similarity1
Metal bindingi151ManganeseBy similarity1
Active sitei240By similarity1
Metal bindingi264ManganeseBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDevelopmental protein, Glycosyltransferase, Transferase
Biological processDifferentiation, Neurogenesis
LigandManganese, Metal-binding

Protein family/group databases

CAZyiGT31 Glycosyltransferase Family 31

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-1,3-N-acetylglucosaminyltransferase radical fringe (EC:2.4.1.222)
Alternative name(s):
O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase
Gene namesi
Name:Rfng
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621322 Rfng

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 6CytoplasmicSequence analysis6
Transmembranei7 – 29Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST23
Topological domaini30 – 334LumenalSequence analysisAdd BLAST305

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002191871 – 334Beta-1,3-N-acetylglucosaminyltransferase radical fringeAdd BLAST334

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi116N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi117 ↔ 128By similarity
Disulfide bondi146 ↔ 210By similarity
Disulfide bondi314 ↔ 323By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9R1U9
PRIDEiQ9R1U9

Expressioni

Tissue specificityi

Most abundantly expressed in adult brain. Expressed in most neurons of the brain but not in glial cells. Also detected to a lower extent in adult lung and kidney.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000067562

Structurei

3D structure databases

ProteinModelPortaliQ9R1U9
SMRiQ9R1U9
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 31 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410II9W Eukaryota
ENOG410XS8Y LUCA
HOVERGENiHBG007986
InParanoidiQ9R1U9
KOiK05948
PhylomeDBiQ9R1U9

Family and domain databases

InterProiView protein in InterPro
IPR017374 Fringe
IPR003378 Fringe-like
PfamiView protein in Pfam
PF02434 Fringe, 1 hit
PIRSFiPIRSF038073 B-acetylgalactosaminyltfrase, 1 hit

Sequencei

Sequence statusi: Complete.

Q9R1U9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRVRRVLCR ACLALAAVLA VLLLLPLPLP LPLPLPRAPA PDPGRVPTGS
60 70 80 90 100
LTLEVSRLQP DDVFIAVKTT RKNHGPRLRL LLRTWISRAP RQTFIFTDGD
110 120 130 140 150
DPELQLLAGS QMINTNCSAV RTRQALCCKM SVEYDKFIES GRKWFCHVDD
160 170 180 190 200
DNYVNPKSLL HLLSTFSSNQ DIYLGRPSLD HPIEATERVQ GGGTSNTVKF
210 220 230 240 250
WFATGGAGFC LSRGLALKMS PWASLGSFMS TAERVRLPDD CTVGYIVEGL
260 270 280 290 300
LGARLLHSPL FHSHLENLQK LPSGAVLQQV TLSYGGPENP HNVVNVAGSF
310 320 330
SIRQDPTRFQ SVHCLLYPDT HWCPMKNRGK EAFQ
Length:334
Mass (Da):36,993
Last modified:May 1, 2000 - v1
Checksum:iED0D21CFD5BFB40A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB016486 mRNA Translation: BAA82742.1
RefSeqiNP_068621.1, NM_021849.1
UniGeneiRn.168817

Genome annotation databases

GeneIDi60433
KEGGirno:60433

Similar proteinsi

Entry informationi

Entry nameiRFNG_RAT
AccessioniPrimary (citable) accession number: Q9R1U9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 10, 2003
Last sequence update: May 1, 2000
Last modified: May 23, 2018
This is version 91 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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